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Protein

Ceramide very long chain fatty acid hydroxylase SCS7

Gene

SCS7

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Ceramide hydroxylase involved in the alpha-hydroxylation of sphingolipid-associated very long chain fatty acids. Hydroxylates the very long chain fatty acid of ceramides at C2 and C3.6 Publications

Cofactori

Fe cationBy similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi45Iron (heme axial ligand)PROSITE-ProRule annotation1
Metal bindingi72Iron (heme axial ligand)PROSITE-ProRule annotation1

GO - Molecular functioni

  • fatty acid alpha-hydroxylase activity Source: SGD
  • heme binding Source: InterPro
  • iron ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Transport

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:YMR272C-MONOMER.
YEAST:YMR272C-MONOMER.
ReactomeiR-SCE-1660661. Sphingolipid de novo biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Ceramide very long chain fatty acid hydroxylase SCS7 (EC:1.-.-.-)
Short name:
Ceramide VLCFA hydroxylase SCS7
Alternative name(s):
Suppressor of calcium sensitivity 7
Gene namesi
Name:SCS7
Synonyms:FAH1
Ordered Locus Names:YMR272C
ORF Names:YM8156.14C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YMR272C.
SGDiS000004885. SCS7.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 196CytoplasmicSequence analysisAdd BLAST196
Transmembranei197 – 217HelicalSequence analysisAdd BLAST21
Topological domaini218 – 222LumenalSequence analysis5
Transmembranei223 – 243HelicalSequence analysisAdd BLAST21
Topological domaini244 – 297CytoplasmicSequence analysisAdd BLAST54
Transmembranei298 – 318HelicalSequence analysisAdd BLAST21
Topological domaini319 – 352LumenalSequence analysisAdd BLAST34
Transmembranei353 – 373HelicalSequence analysisAdd BLAST21
Topological domaini374 – 384CytoplasmicSequence analysisAdd BLAST11

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001854071 – 384Ceramide very long chain fatty acid hydroxylase SCS7Add BLAST384

Proteomic databases

MaxQBiQ03529.
PRIDEiQ03529.

PTM databases

iPTMnetiQ03529.

Interactioni

Protein-protein interaction databases

BioGridi35451. 528 interactors.
IntActiQ03529. 34 interactors.
MINTiMINT-4498866.

Structurei

Secondary structure

1384
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi129 – 132Combined sources4
Helixi138 – 145Combined sources8
Helixi154 – 159Combined sources6
Helixi165 – 172Combined sources8
Helixi191 – 194Combined sources4
Helixi200 – 219Combined sources20
Helixi222 – 246Combined sources25
Turni247 – 249Combined sources3
Helixi251 – 253Combined sources3
Helixi258 – 267Combined sources10
Helixi269 – 273Combined sources5
Beta strandi280 – 282Combined sources3
Helixi285 – 302Combined sources18
Helixi305 – 330Combined sources26
Helixi336 – 350Combined sources15
Beta strandi353 – 355Combined sources3
Helixi363 – 367Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4ZR0X-ray3.80A/B1-384[»]
4ZR1X-ray2.60A/B96-384[»]
ProteinModelPortaliQ03529.
SMRiQ03529.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini9 – 90Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd BLAST82

Domaini

The histidine box domains may contain the active site and/or be involved in metal ion binding.

Sequence similaritiesi

Contains 1 cytochrome b5 heme-binding domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00390000002142.
HOGENOMiHOG000023981.
InParanoidiQ03529.
KOiK19703.
OMAiVHPRTGM.
OrthoDBiEOG092C3MYJ.

Family and domain databases

Gene3Di3.10.120.10. 1 hit.
InterProiIPR001199. Cyt_B5-like_heme/steroid-bd.
IPR018506. Cyt_B5_heme-BS.
IPR006694. Fatty_acid_hydroxylase.
IPR014430. Scs7.
[Graphical view]
PfamiPF00173. Cyt-b5. 1 hit.
PF04116. FA_hydroxylase. 1 hit.
[Graphical view]
PIRSFiPIRSF005149. IPC-B_HD. 1 hit.
PRINTSiPR00363. CYTOCHROMEB5.
SMARTiSM01117. Cyt-b5. 1 hit.
[Graphical view]
SUPFAMiSSF55856. SSF55856. 1 hit.
PROSITEiPS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q03529-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTNTSKTLE LFSKKTVQEH NTANDCWVTY QNRKIYDVTR FLSEHPGGDE
60 70 80 90 100
SILDYAGKDI TEIMKDSDVH EHSDSAYEIL EDEYLIGYLA TDEEAARLLT
110 120 130 140 150
NKNHKVEVQL SADGTEFDST TFVKELPAEE KLSIATDYSN DYKKHKFLDL
160 170 180 190 200
NRPLLMQILR SDFKKDFYVD QIHRPRHYGK GSAPLFGNFL EPLTKTAWWV
210 220 230 240 250
VPVAWLPVVV YHMGVALKNM NQLFACFLFC VGVFVWTLIE YGLHRFLFHF
260 270 280 290 300
DDWLPESNIA FATHFLLHGC HHYLPMDKYR LVMPPTLFVI LCAPFYKLVF
310 320 330 340 350
ALLPLYWAYA GFAGGLFGYV CYDECHFFLH HSKLPPFMRK LKKYHLEHHY
360 370 380
KNYQLGFGVT SWFWDEVFGT YLGPDAPLSK MKYE
Length:384
Mass (Da):44,881
Last modified:November 1, 1997 - v1
Checksum:iDF4BA5F2E0EA2218
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49260 Genomic DNA. Translation: CAA89255.1.
AY693150 Genomic DNA. Translation: AAT93169.1.
BK006946 Genomic DNA. Translation: DAA10172.1.
PIRiS54484.
RefSeqiNP_013999.1. NM_001182779.1.

Genome annotation databases

EnsemblFungiiYMR272C; YMR272C; YMR272C.
GeneIDi855315.
KEGGisce:YMR272C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49260 Genomic DNA. Translation: CAA89255.1.
AY693150 Genomic DNA. Translation: AAT93169.1.
BK006946 Genomic DNA. Translation: DAA10172.1.
PIRiS54484.
RefSeqiNP_013999.1. NM_001182779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4ZR0X-ray3.80A/B1-384[»]
4ZR1X-ray2.60A/B96-384[»]
ProteinModelPortaliQ03529.
SMRiQ03529.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35451. 528 interactors.
IntActiQ03529. 34 interactors.
MINTiMINT-4498866.

PTM databases

iPTMnetiQ03529.

Proteomic databases

MaxQBiQ03529.
PRIDEiQ03529.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYMR272C; YMR272C; YMR272C.
GeneIDi855315.
KEGGisce:YMR272C.

Organism-specific databases

EuPathDBiFungiDB:YMR272C.
SGDiS000004885. SCS7.

Phylogenomic databases

GeneTreeiENSGT00390000002142.
HOGENOMiHOG000023981.
InParanoidiQ03529.
KOiK19703.
OMAiVHPRTGM.
OrthoDBiEOG092C3MYJ.

Enzyme and pathway databases

BioCyciMetaCyc:YMR272C-MONOMER.
YEAST:YMR272C-MONOMER.
ReactomeiR-SCE-1660661. Sphingolipid de novo biosynthesis.

Miscellaneous databases

PROiQ03529.

Family and domain databases

Gene3Di3.10.120.10. 1 hit.
InterProiIPR001199. Cyt_B5-like_heme/steroid-bd.
IPR018506. Cyt_B5_heme-BS.
IPR006694. Fatty_acid_hydroxylase.
IPR014430. Scs7.
[Graphical view]
PfamiPF00173. Cyt-b5. 1 hit.
PF04116. FA_hydroxylase. 1 hit.
[Graphical view]
PIRSFiPIRSF005149. IPC-B_HD. 1 hit.
PRINTSiPR00363. CYTOCHROMEB5.
SMARTiSM01117. Cyt-b5. 1 hit.
[Graphical view]
SUPFAMiSSF55856. SSF55856. 1 hit.
PROSITEiPS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSCS7_YEAST
AccessioniPrimary (citable) accession number: Q03529
Secondary accession number(s): D6W098
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 151 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 3290 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.